ID A0A3Q1FK06_9TELE Unreviewed; 1660 AA.
AC A0A3Q1FK06;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Vitellogenin-1-like {ECO:0000313|Ensembl:ENSAPOP00000018306.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018306.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000018306.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR Ensembl; ENSAPOT00000027853.1; ENSAPOP00000018306.1; ENSAPOG00000021867.1.
DR GeneTree; ENSGT00530000064273; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 1.
DR Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 2.
DR Gene3D; 2.20.90.10; Vitellinogen, beta-sheet shell domain; 1.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015258; Vitellinogen_b-sht_shell.
DR InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR PANTHER; PTHR23345:SF9; VTG7 PROTEIN-RELATED; 1.
DR Pfam; PF09175; Vit_b-sht_shell; 1.
DR Pfam; PF09172; Vit_open_b-sht; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM01170; DUF1944; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00557}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018764648"
FT DOMAIN 24..659
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1395..1570
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 1074..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 162..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
FT DISULFID 204..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 1660 AA; 185025 MW; 144B3CA10F36BD86 CRC64;
MRAVVLALTV AFVGDETVLT ALEFAAGKTY IYKYETLILG GLPEEGLARA GLNFTSKVLI
SAQGQNNYML KLEDYAFYEY NGIWPQEKFV KASTLTSELK SQFDKAIKFE YAGGMVDKMY
APLEVSPMVL NIYRGILGVL QLNIKKTHNV YELQEAGTQG ICKTLYAISE DEKAERILLT
KTRDMNHCQE KIIMDMGLAY MEKCVKCQED IKNLRGTTTY SYVLKEVEGG VELREVRAFE
LIQFSPFSEK KGAAQMETRQ SLIFKEYRQI GMQPISAQYV HHGSLKYEIP TDLIHTPIQM
NKTSSVVQID EILKHLVSHN EETVHEDAPM KFVELFQLLR KMKHEDLANL WKKYINMPVY
RRWLLDSITV TATPASLQFF KDQLLPSILE VAQALIGSIH MVTASNESLE LFRMVINNKQ
FMEKPIQREI LLLGYGTMIY RHCSEMTACS PELLKVRKIW VFFHASAKFW EENVILYLKA
LGNAGHPASL KKISKYLPIH GTAAANQPTK VHAEAIMAMR NIAKKEPRMV QEYALQLFMD
SALPPELRML SCIVMFETRP PIALVITLAN IVKREKNLQV ASFTYSHMKS LTRSTSPIHA
PLAAACNVAL KILGPQLDRL SMRYSRAIHM ETYSSPYMLG AAASAFYIND AATILPKSIM
AKTRAYIAGA AADILEVGVR TEGLQEALLK NPSLLDNADR INKMKRVISA LSQWRSQPNS
KPLASFYVKL FGQEVAYANI DKTLVNQAIE VRVQQPLVNF NAVQTLQDGA SYHFAKPLLI
TEVRRILPTI AGIPMELSLY TAAVTAAKIK VSASITPALP DNFALADLWQ KDIRLSTEIR
PSAVANSFAV MGVNTAYIQA ALVTRAKLNF TSPVKIGASF NMQEESFKIE ALPVSVPEPF
AAAEVESFAT TRMNDETAPK LTPIIPIKRS KSRSTEILTS KVASSAVVSV SKSSEILSQE
EQAARQNQSR VLKKKYCAKM VGVGLKACFK VATQNVSYLQ DTPLYKAAGR YAVALSFKPI
EGETVERLEM EVAVGQRAAE KLIKQITVSQ EAIREGRPIL MKLKRILVPN AGNSSSSRFS
SSKSSSSSSS SRPSSKVNDT AVQLVKHHRS HRSSSSSSSS SSSRSSSSSS SSSSSSSSXX
XXXXXXXXXX XXXXSSRSSS RSHSSVRSRF RSSSSSSASS LASLFSGSSS SSSSSSRHSR
NKFLGSEAAI LAVVFRAVKE NKKMQGYQVA TYLDKPTARL QVILAPLAVD SKWKICADGV
LSSKHKAMAR FSWGPECSKY NTTVTVETGL VGKKPAARIR VQWKRIPSTM KHYAKMAFKG
IPSRMLSDLF RGKDRNSTKQ ISLTVFRASN RSLEFIWKTL RHNVYRLHLP INLPFDIRHI
FNDSIDDIIS HAGAAECLSS QDTIKTFNNR TYSNKTPQSC YQILAADCTQ DLKFIVLLKK
DAQEHNHINI KIADIDVDLY PKDGQVVVEV NSREMPIRSQ SYQHPTEDIR IRQIGEGISV
VAPKYGLTEV YFEKNSWKIK VADWMKGQTC GLCGKADGEI RQEYRTPSGR LAKNEESHAL
SWVVPGKSCR DANECRLKHE SVRLEKQVNI HGQNTKCYSV EPVLRCLPGC YPVNTSKVNV
GFHCLPTEAN LNTVNMYERS EDLREYADAH TACRCTAQCI
//
